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Database: UniProt
Entry: W9HXA6_FUSOX
LinkDB: W9HXA6_FUSOX
Original site: W9HXA6_FUSOX 
ID   W9HXA6_FUSOX            Unreviewed;      1002 AA.
AC   W9HXA6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=FOYG_12784 {ECO:0000313|EMBL:EWY85650.1};
OS   Fusarium oxysporum FOSC 3-a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=909455 {ECO:0000313|EMBL:EWY85650.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY85650.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|EMBL:EWY85650.1,
RC   ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L.,
RA   Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; JH717846; EWY85650.1; -; Genomic_DNA.
DR   EnsemblFungi; EWY85650; EWY85650; FOYG_12784.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030753};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18   1002       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004922321.
FT   DOMAIN      389    565       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1002 AA;  109934 MW;  016B39C3CC8946B8 CRC64;
     MKLSNFLLAA LAASTHAQNV FPRGTRPSNI LDSRALLQDI VTFDEHSLFI HGERVTIFSA
     EIHPFRLPVA SLYPDLFQKV KAMGFNMVSF YVDWALLEGK PGEFRSEGAL DLQPFIDAAH
     EAGIYLLARP GPYINAEVSG GGFPGWLQRV KGFLRTNATD YLAATDNYVA HVAKIIAKAQ
     ITNGGPVILY QPENEYSAAQ GTPFPNHDYL KYVNDQVRKA GVVVPLINND AWQGGTGAPG
     TGPGAVDIYG HDGYPVGFDC ANPYTWPKDG LPTTWHAEHE KISPNTPYSI IEFQGGGFDP
     PGGGGFDNCY ELTNHEFARI FYKNNLAAGV TIFNIYMTWG GTNWGNLGHS DGYTSYDYGA
     AIKEDRTITR EKYSEIKLQG QFLRVSPNYA IAEASNFTTT KYTDNKNIAV TALNTKKDDA
     FYVVRHADYR TTDSASYKLK VKTSTGTLTI PQLGGSLSLH RRDSKIHVVD YPVGKFKLLY
     STAEVFTWKV LGDKTVLVLY GGADEVHEVA VKGQEKVKVV EGDGVKIEKK SGAGVFQFKT
     STKRRVVQAG SLYIYLLDRN AAYKYWVPTI PSKKSGAYGS SVMNPDAVII NGPYLVRSVA
     VEGSKLSVQA DFNITTPVEI IGTSKGTSRL SINGKGTSFT KSKLGNWLVN PEIKLPTAKV
     PDVKSLDWHY IDGLPEVKKD YDDSKWRTAD IKKTLNSKWP LHNSVSLYSG DYGFNAGALI
     FRGHFTASGS ESKLKLWTFG GRAYGSSVWL DDKFVGSVTG GGNNNNDTST YKLPKTERGK
     KHVVTVIVDN MGLNGNWVPG VDETKQPRGI LDWHITSDSG KETKVSKWKL TGNLGGENYK
     DKFRGPLNEG GFFFERQGYH LPSPPLTSFK SGSPFKGLSK PGVSFYTAKL PLNLPSSTHD
     IPLSFTFKNN TSSTGAYRAI LYVNGFQYGK YVANVGPQTV FPVPEGILNY KGDNWIGIAL
     WALEKSANVD GLSLTAGVAV QTGRKPVKVV EGPKYSRRQD AY
//
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